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Cardiac Hypertrophy, Heart Failure and Cardiomyopathy
Published in Mary N. Sheppard, Practical Cardiovascular Pathology, 2022
The X-linked gene responsible for Emery-Dreifuss muscular dystrophy, emerin (another nuclear lamin protein), causes similar clinical features. Other DCM genes of this type include desmin, caveolin and α- and β-sarcoglycan, as well as the mitochondrial respiratory chain gene. X-linked DCM is also caused by the Duchenne muscular dystrophy dystrophin gene, whereas G 4.5 (tafazzin), causes Barth syndrome, which is an X-linked cardioskeletal myopathy in infants.22
Muscle Disorders
Published in Philip B. Gorelick, Fernando D. Testai, Graeme J. Hankey, Joanna M. Wardlaw, Hankey's Clinical Neurology, 2020
Kourosh Rezania, Peter Pytel, Betty Soliven
Lamin A/C and emerin are part of the inner nuclear envelope. They are thought to have a role in maintaining nuclear shape and to be important for scaffolding DNA in the nucleus. Through DNA binding, these proteins may influence gene expression.
Neuromuscular disorders
Published in Angus Clarke, Alex Murray, Julian Sampson, Harper's Practical Genetic Counselling, 2019
This is often X-linked, determined by a specific gene for the protein ‘emerin’, allowing specific mutation testing in some families. Affected males and some carrier females are at risk of serious cardiac conduction defects, even though weakness is often mild. Some clinically similar families follow autosomal dominant inheritance, and the disorder is due to defects in the gene LMNA, encoding the muscle proteins lamin A and lamin C. This is an unusual gene in which mutations can cause a very wide range of different phenotypes including lipodystrophy and progeria as well as muscular dystrophy.
What can we learn from senescent platelets, their transcriptomes and proteomes?
Published in Platelets, 2023
Harriet E. Allan, Ami Vadgama, Paul C. Armstrong, Timothy D. Warner
Against a background of protein loss, a number of cytoskeletal-associated proteins such as Emerin, Gelsolin and Twinfilin-2 were lost to a greater extent.5 This accelerated loss of cytoskeletal proteins is of particular interest as the cytoskeleton is fundamental during platelet activation and its rearrangement underpins all stages of adhesion and aggregation. Furthermore, a platelet-specific knockout mouse model of Twinfilin-2a showed an increase in platelet turnover, suggesting that the cytoskeleton and associated proteins are important in determining platelet life span.48 In addition, aged platelets also have a significant reduction in mitochondrial-associated proteins, suggesting that platelet aging may be accompanied by changes in metabolism.5 Consistent with a loss of organelles in aged platelets, a number of proteins traditionally associated with the endoplasmic reticulum and Golgi apparatus including Reticulon-1, Inverted Formin-2 and Extended Synaptotagmin-1 were found to be reduced in aged platelets, indicating their inheritance from precursor megakaryocytes as these structures are largely lacking from platelets.5